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Conserved domains on  [gi|1336550306|gb|AUV81077|]
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competence protein [Salinigranum rubrum]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11457104)

uncharacterized member of the MBL fold metallo-hydrolase superfamily similar to the phosphorylcholine esterase (Pce) domain of choline-binding protein e from Streptococcus pneumoniae

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 61-315 1.50e-83

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


:

Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 257.86  E-value: 1.50e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  61 LEVHFINVGQGDSTLIVGPTGETVLVDTG---DFRDDGAYVVDYLQSRGIDRIDALVSTHADADHIGGHAAVIEHFEteg 137
Cdd:COG2333     1 LRVTFLDVGQGDAILIRTPDGKTILIDTGprpSFDAGERVVLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEAFP--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 138 egVGAVYDPGVAASTATYDRYLDAVERHDVPLYRTLAGDRIPLDGARVTVLGPPQTPLADGERNENSIVLRVEFGRTSVL 217
Cdd:COG2333    78 --VGRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQLGGVRFEVLWPPEDLLEGSDENNNSLVLRLTYGGFSFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 218 LPGDAGPVEEPYLVDNHEEaLDVTLLKAGHHGSSSSTSAALLNAATPKAVVVSSAYDSRYGHPHEEVLGRLASRSIPTYW 297
Cdd:COG2333   156 LTGDAEAEAEAALLARGPD-LKADVLKVPHHGSKTSSSPAFLEAVRPRVAVISVGRDNRYGHPHPEVLERLRAAGIRVYR 234

                         250
                  ....*....|....*...
gi 1336550306 298 TATHGTVVATSDGTAVEV 315
Cdd:COG2333   235 TDRDGAITVTSDGDGLRV 252
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 358-470 1.65e-32

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


:

Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 119.45  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 358 VPTGARIDVSEIHADAAGDdaenlADEYVVVTNRGSEPVDLSGWVLTDESGARYTFPSNTVLAPGDSLTVRTGDGTDTAT 437
Cdd:pfam00932   1 SSATGDVVISEVVYDGSGG-----NDEFIELYNTGSKAVDLSGWKLQDASGGTYTFPNGTTLAPGQTVVVWTGSGTNSAT 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1336550306 438 DRYWDAGRPVWNNDGDTVTLLRPDGGVVTEVSY 470
Cdd:pfam00932  76 AGYWGPSNAVWNNGGDAVALYDANGELVDSVGY 108
 
Name Accession Description Interval E-value
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 61-315 1.50e-83

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 257.86  E-value: 1.50e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  61 LEVHFINVGQGDSTLIVGPTGETVLVDTG---DFRDDGAYVVDYLQSRGIDRIDALVSTHADADHIGGHAAVIEHFEteg 137
Cdd:COG2333     1 LRVTFLDVGQGDAILIRTPDGKTILIDTGprpSFDAGERVVLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEAFP--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 138 egVGAVYDPGVAASTATYDRYLDAVERHDVPLYRTLAGDRIPLDGARVTVLGPPQTPLADGERNENSIVLRVEFGRTSVL 217
Cdd:COG2333    78 --VGRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQLGGVRFEVLWPPEDLLEGSDENNNSLVLRLTYGGFSFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 218 LPGDAGPVEEPYLVDNHEEaLDVTLLKAGHHGSSSSTSAALLNAATPKAVVVSSAYDSRYGHPHEEVLGRLASRSIPTYW 297
Cdd:COG2333   156 LTGDAEAEAEAALLARGPD-LKADVLKVPHHGSKTSSSPAFLEAVRPRVAVISVGRDNRYGHPHPEVLERLRAAGIRVYR 234

                         250
                  ....*....|....*...
gi 1336550306 298 TATHGTVVATSDGTAVEV 315
Cdd:COG2333   235 TDRDGAITVTSDGDGLRV 252
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 62-245 4.10e-62

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 199.67  E-value: 4.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  62 EVHFINVGQGDSTLIVGPtGETVLVDTGD-FRDDGAYVVDYLQSRGIDRIDALVSTHADADHIGGHAAVIEHFEtegegV 140
Cdd:cd07731     1 RVHFLDVGQGDAILIQTP-GKTILIDTGPrDSFGEDVVVPYLKARGIKKLDYLILTHPDADHIGGLDAVLKNFP-----V 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 141 GAVYDPGVAASTATYDRYLDAVERHDVPLYRTLAGDRIPLDGARVTVLGPPQTPLADGerNENSIVLRVEFGRTSVLLPG 220
Cdd:cd07731    75 KEVYMPGVTHTTKTYEDLLDAIKEKGIPVTPCKAGDRWQLGGVSFEVLSPPKDDYDDL--NNNSCVLRLTYGGTSFLLTG 152

                         170       180
                  ....*....|....*....|....*
gi 1336550306 221 DAGPVEEPYLVDNHEEaLDVTLLKA 245
Cdd:cd07731   153 DAEKEAEEELLASGPD-LLADVLKV 176
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 358-470 1.65e-32

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 119.45  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 358 VPTGARIDVSEIHADAAGDdaenlADEYVVVTNRGSEPVDLSGWVLTDESGARYTFPSNTVLAPGDSLTVRTGDGTDTAT 437
Cdd:pfam00932   1 SSATGDVVISEVVYDGSGG-----NDEFIELYNTGSKAVDLSGWKLQDASGGTYTFPNGTTLAPGQTVVVWTGSGTNSAT 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1336550306 438 DRYWDAGRPVWNNDGDTVTLLRPDGGVVTEVSY 470
Cdd:pfam00932  76 AGYWGPSNAVWNNGGDAVALYDANGELVDSVGY 108
ComEC_Rec2 TIGR00361
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ...
 60-302 1.42e-17

DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 species so far (Haemophilus influenzae, Escherichia coli, Bacillus subtilis, Neisseria gonorrhoeae, Streptococcus pneumoniae), of which all but E. coli are model systems for the study of competence for natural transformation. This protein is a predicted multiple membrane-spanning protein likely to be involved in DNA internalization. In a large number of bacterial species not known to exhibit competence, this protein is replaced by a half-length N-terminal homolog of unknown function, modelled by the related model ComEC_N-term. The role for this protein in species that are not naturally transformable is unknown. [Cellular processes, DNA transformation]


Pssm-ID: 273036 [Multi-domain]  Cd Length: 662  Bit Score: 85.33  E-value: 1.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  60 TLEVHFINVGQGDSTLIVGPtGETVLVDTGDFRDDGAY----VVDYLQSRGIdRIDALVSTHADADHIGGHAAVIEHFet 135
Cdd:TIGR00361 439 SWQVDMLDVGQGLAMFIGAN-GKGILYDTGEPWREGSLgekvIIPFLTAKGI-KLEALILSHADQDHIGGAEIILKHH-- 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 136 egegvgavydPGVAASTATYDRYldaVERHDVPLYRtlaGDRIPLDGARVTVLGPPQTPLADGerNENSIVLRVEFGRTS 215
Cdd:TIGR00361 515 ----------PVKRLVIPKGFVE---EGVAIEECKR---GDVWQWQGLQFHVLSPEAPDPASK--NNHSCVLWVDDGGNS 576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 216 VLLPGDA-GPVEEpyLVDNHEEALDVTLLKAGHHGSSSSTSAALLNAATPKAVVVSSAYDSRYGHPHEEVLGRLASRSIP 294
Cdd:TIGR00361 577 WLLTGDLeAEGEQ--EVMRVFPNIKADVLQVGHHGSKTSTSEELIQQVQPKVAIISAGRNNRWHHPHQKVLQRLQRHSIR 654


                  ....*...
gi 1336550306 295 TYWTATHG 302
Cdd:TIGR00361 655 VLRTDQNG 662
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
66-232 7.86e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.09  E-value: 7.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  66 INVGQGDSTLIVGPtGETVLVDTGDFRDDGAYVVDYLQSRGIDRIDALVSTHADADHIGGHAAVIEHFetegeGVGAVYD 145
Cdd:pfam00753   1 LGPGQVNSYLIEGG-GGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEAT-----DVPVIVV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 146 PGVAAStATYDRYLDAVERHDVPLYRTLAGDRIPLDGARVTVLGPPQTPLADGERNENSIVLRVEFGRTSVLLPGDAGPV 225
Cdd:pfam00753  75 AEEARE-LLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFA 153


                  ....*..
gi 1336550306 226 EEPYLVD 232
Cdd:pfam00753 154 GEIGRLD 160
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 73-228 1.35e-11

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 62.96  E-value: 1.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306   73 STLIVGPtGETVLVDTGDFRDDGayVVDYLQSRGIDRIDALVSTHADADHIGGHAAVIEHFETEgegvgavydpgVAAST 152
Cdd:smart00849   2 SYLVRDD-GGAILIDTGPGEAED--LLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAP-----------VYAPE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  153 ATYDRYLDAVERHDVPLYRTLA---------GDRIPLDGARVTVLGPP-QTPladgerneNSIVLRVEFGRtsVLLPGDA 222
Cdd:smart00849  68 GTAELLKDLLALLGELGAEAEPappdrtlkdGDELDLGGGELEVIHTPgHTP--------GSIVLYLPEGK--ILFTGDL 137


                   ....*.
gi 1336550306  223 GPVEEP 228
Cdd:smart00849 138 LFAGGD 143
PRK11539 PRK11539
ComEC family competence protein; Provisional
 63-310 8.70e-04

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 41.90  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  63 VHFINVGQGDSTLIVgPTGETVLVDTGDFRDDGA----YVVDYLQSRGIDrIDALVSTHADADHIGGHAAVIEHFetege 138
Cdd:PRK11539  503 VDMLDVGHGLAVVIE-RNGKAILYDTGNAWPTGDsaqqVIIPWLRWHGLT-PEGIILSHEHLDHRGGLASLLHAW----- 575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 139 gvgavydPGVAASTATYdryldavERHDVPLYRtlaGDRIPLDGARVTVLGPPQTPLADGerNENSIVLRVEFGRTSVLL 218
Cdd:PRK11539  576 -------PMAWIRSPLN-------WANHLPCVR---GEQWQWQGLTFSVHWPLEQSNDAG--NNDSCVIRVDDGKHSILL 636

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 219 PGDAGPVEEPYLVDNHEEALDVTLLKAGHHGSSSSTSAALLNAATPKAVVVSSAYDSRYGHPHEEVLGRLASRSIPTYWT 298
Cdd:PRK11539  637 TGDLEAQAEQKLLSRYWQQLAATLLQVPHHGSNTSSSLPFIRAVNGKVALASASRYNAWRLPSVKVKQRYQQQGYQWRDT 716

                         250
                  ....*....|....
gi 1336550306 299 ATHG--TVVATSDG 310
Cdd:PRK11539  717 PHSGqlSVYFSADG 730
 
Name Accession Description Interval E-value
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 61-315 1.50e-83

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 257.86  E-value: 1.50e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  61 LEVHFINVGQGDSTLIVGPTGETVLVDTG---DFRDDGAYVVDYLQSRGIDRIDALVSTHADADHIGGHAAVIEHFEteg 137
Cdd:COG2333     1 LRVTFLDVGQGDAILIRTPDGKTILIDTGprpSFDAGERVVLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEAFP--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 138 egVGAVYDPGVAASTATYDRYLDAVERHDVPLYRTLAGDRIPLDGARVTVLGPPQTPLADGERNENSIVLRVEFGRTSVL 217
Cdd:COG2333    78 --VGRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQLGGVRFEVLWPPEDLLEGSDENNNSLVLRLTYGGFSFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 218 LPGDAGPVEEPYLVDNHEEaLDVTLLKAGHHGSSSSTSAALLNAATPKAVVVSSAYDSRYGHPHEEVLGRLASRSIPTYW 297
Cdd:COG2333   156 LTGDAEAEAEAALLARGPD-LKADVLKVPHHGSKTSSSPAFLEAVRPRVAVISVGRDNRYGHPHPEVLERLRAAGIRVYR 234

                         250
                  ....*....|....*...
gi 1336550306 298 TATHGTVVATSDGTAVEV 315
Cdd:COG2333   235 TDRDGAITVTSDGDGLRV 252
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 62-245 4.10e-62

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 199.67  E-value: 4.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  62 EVHFINVGQGDSTLIVGPtGETVLVDTGD-FRDDGAYVVDYLQSRGIDRIDALVSTHADADHIGGHAAVIEHFEtegegV 140
Cdd:cd07731     1 RVHFLDVGQGDAILIQTP-GKTILIDTGPrDSFGEDVVVPYLKARGIKKLDYLILTHPDADHIGGLDAVLKNFP-----V 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 141 GAVYDPGVAASTATYDRYLDAVERHDVPLYRTLAGDRIPLDGARVTVLGPPQTPLADGerNENSIVLRVEFGRTSVLLPG 220
Cdd:cd07731    75 KEVYMPGVTHTTKTYEDLLDAIKEKGIPVTPCKAGDRWQLGGVSFEVLSPPKDDYDDL--NNNSCVLRLTYGGTSFLLTG 152

                         170       180
                  ....*....|....*....|....*
gi 1336550306 221 DAGPVEEPYLVDNHEEaLDVTLLKA 245
Cdd:cd07731   153 DAEKEAEEELLASGPD-LLADVLKV 176
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 358-470 1.65e-32

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 119.45  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 358 VPTGARIDVSEIHADAAGDdaenlADEYVVVTNRGSEPVDLSGWVLTDESGARYTFPSNTVLAPGDSLTVRTGDGTDTAT 437
Cdd:pfam00932   1 SSATGDVVISEVVYDGSGG-----NDEFIELYNTGSKAVDLSGWKLQDASGGTYTFPNGTTLAPGQTVVVWTGSGTNSAT 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1336550306 438 DRYWDAGRPVWNNDGDTVTLLRPDGGVVTEVSY 470
Cdd:pfam00932  76 AGYWGPSNAVWNNGGDAVALYDANGELVDSVGY 108
ComEC_Rec2 TIGR00361
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ...
 60-302 1.42e-17

DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 species so far (Haemophilus influenzae, Escherichia coli, Bacillus subtilis, Neisseria gonorrhoeae, Streptococcus pneumoniae), of which all but E. coli are model systems for the study of competence for natural transformation. This protein is a predicted multiple membrane-spanning protein likely to be involved in DNA internalization. In a large number of bacterial species not known to exhibit competence, this protein is replaced by a half-length N-terminal homolog of unknown function, modelled by the related model ComEC_N-term. The role for this protein in species that are not naturally transformable is unknown. [Cellular processes, DNA transformation]


Pssm-ID: 273036 [Multi-domain]  Cd Length: 662  Bit Score: 85.33  E-value: 1.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  60 TLEVHFINVGQGDSTLIVGPtGETVLVDTGDFRDDGAY----VVDYLQSRGIdRIDALVSTHADADHIGGHAAVIEHFet 135
Cdd:TIGR00361 439 SWQVDMLDVGQGLAMFIGAN-GKGILYDTGEPWREGSLgekvIIPFLTAKGI-KLEALILSHADQDHIGGAEIILKHH-- 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 136 egegvgavydPGVAASTATYDRYldaVERHDVPLYRtlaGDRIPLDGARVTVLGPPQTPLADGerNENSIVLRVEFGRTS 215
Cdd:TIGR00361 515 ----------PVKRLVIPKGFVE---EGVAIEECKR---GDVWQWQGLQFHVLSPEAPDPASK--NNHSCVLWVDDGGNS 576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 216 VLLPGDA-GPVEEpyLVDNHEEALDVTLLKAGHHGSSSSTSAALLNAATPKAVVVSSAYDSRYGHPHEEVLGRLASRSIP 294
Cdd:TIGR00361 577 WLLTGDLeAEGEQ--EVMRVFPNIKADVLQVGHHGSKTSTSEELIQQVQPKVAIISAGRNNRWHHPHQKVLQRLQRHSIR 654


                  ....*...
gi 1336550306 295 TYWTATHG 302
Cdd:TIGR00361 655 VLRTDQNG 662
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
66-232 7.86e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.09  E-value: 7.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  66 INVGQGDSTLIVGPtGETVLVDTGDFRDDGAYVVDYLQSRGIDRIDALVSTHADADHIGGHAAVIEHFetegeGVGAVYD 145
Cdd:pfam00753   1 LGPGQVNSYLIEGG-GGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEAT-----DVPVIVV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 146 PGVAAStATYDRYLDAVERHDVPLYRTLAGDRIPLDGARVTVLGPPQTPLADGERNENSIVLRVEFGRTSVLLPGDAGPV 225
Cdd:pfam00753  75 AEEARE-LLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFA 153


                  ....*..
gi 1336550306 226 EEPYLVD 232
Cdd:pfam00753 154 GEIGRLD 160
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 73-228 1.35e-11

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 62.96  E-value: 1.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306   73 STLIVGPtGETVLVDTGDFRDDGayVVDYLQSRGIDRIDALVSTHADADHIGGHAAVIEHFETEgegvgavydpgVAAST 152
Cdd:smart00849   2 SYLVRDD-GGAILIDTGPGEAED--LLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAP-----------VYAPE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  153 ATYDRYLDAVERHDVPLYRTLA---------GDRIPLDGARVTVLGPP-QTPladgerneNSIVLRVEFGRtsVLLPGDA 222
Cdd:smart00849  68 GTAELLKDLLALLGELGAEAEPappdrtlkdGDELDLGGGELEVIHTPgHTP--------GSIVLYLPEGK--ILFTGDL 137


                   ....*.
gi 1336550306  223 GPVEEP 228
Cdd:smart00849 138 LFAGGD 143
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 61-222 4.46e-11

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 62.40  E-value: 4.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  61 LEVHFINVGQGDSTLIVGPTGETVLVDTGDFRDDGAYVVDYLQSRGiDRIDALVSTHADADHIGGHAAVIEHFETEgegv 140
Cdd:COG0491     4 LPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALG-LDIKAVLLTHLHPDHVGGLAALAEAFGAP---- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 141 gaVYDPGVAASTATYDRYLDAVERHDVPLYRTLA-GDRIPLDGARVTVL-GPPQTPladgerneNSIVLRVEFGRtsVLL 218
Cdd:COG0491    79 --VYAHAAEAEALEAPAAGALFGREPVPPDRTLEdGDTLELGGPGLEVIhTPGHTP--------GHVSFYVPDEK--VLF 146


                  ....
gi 1336550306 219 PGDA 222
Cdd:COG0491   147 TGDA 150
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 64-188 2.25e-08

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 53.83  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  64 HFINVGQGDST--LIVGPTGETVLVDTGDfrDDGAYVVDYLQSRGIDrIDALVSTHADADHIGGHAAVIEHFETEgegvg 141
Cdd:cd06262     1 KRLPVGPLQTNcyLVSDEEGEAILIDPGA--GALEKILEAIEELGLK-IKAILLTHGHFDHIGGLAELKEAPGAP----- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1336550306 142 avydpgVAASTATYDRYLDAVERHDVPLYRTLA----------GDRIPLDGARVTVL 188
Cdd:cd06262    73 ------VYIHEADAELLEDPELNLAFFGGGPLPppepdilledGDTIELGGLELEVI 123
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 65-136 3.61e-06

uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 47.60  E-value: 3.61e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336550306  65 FINVgqgdsTLIVGPtGETVLVDTGdFRDDGAYVVDYLQSRGID--RIDALVSTHADADHIGGHAAVIEHFETE 136
Cdd:cd07721    10 PVNA-----YLIEDD-DGLTLIDTG-LPGSAKRILKALRELGLSpkDIRRILLTHGHIDHIGSLAALKEAPGAP 76
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 75-188 5.97e-06

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 46.30  E-value: 5.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  75 LIVGP-TGETVLVDTGDFrddgAYVVDYLQSRGIdRIDALVSTHADADHIGGHAAVIEHFetegeGVGAVYDPgvaasta 153
Cdd:cd07723    13 LIVDEaTGEAAVVDPGEA----EPVLAALEKNGL-TLTAILTTHHHWDHTGGNAELKALF-----PDAPVYGP------- 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1336550306 154 tydrYLDAVERHDVPLYrtlAGDRIPLDGARVTVL 188
Cdd:cd07723    76 ----AEDRIPGLDHPVK---DGDEIKLGGLEVKVL 103
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 81-125 7.24e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 46.70  E-value: 7.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1336550306  81 GETVLVDTG-DFRddgayvvdyLQS--RGIDRIDALVSTHADADHIGG 125
Cdd:cd16279    44 GKNILIDTGpDFR---------QQAlrAGIRKLDAVLLTHAHADHIHG 82
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 70-191 2.17e-05

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 45.22  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  70 QGDSTLIVGPTGETVLVDTGDFRDD-GAYVVDYLQSRGIDRIDALVSTHADADHIGGHAAVIEHFetegegvgavYDPGV 148
Cdd:cd07722    16 QGTNTYLVGTGKRRILIDTGEGRPSyIPLLKSVLDSEGNATISDILLTHWHHDHVGGLPDVLDLL----------RGPSP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1336550306 149 AASTATYDRYLDAVERHDVPLYRTLAGDRIPLDGARVTVLGPP 191
Cdd:cd07722    86 RVYKFPRPEEDEDPDEDGGDIHDLQDGQVFKVEGATLRVIHTP 128
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 67-136 3.50e-05

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 44.44  E-value: 3.50e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  67 NVGqgdstLIVGPTGETVLVDTGDFRDDGAYVVDYLQSRGIdRIDALVSTHADADHIGGHAAVIEHFETE 136
Cdd:cd07743     9 NIG-----VYVFGDKEALLIDSGLDEDAGRKIRKILEELGW-KLKAIINTHSHADHIGGNAYLQKKTGCK 72
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 75-239 8.39e-05

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 44.13  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  75 LIVGPTGeTVLVDTG---DFRDDGAY--------------VVDYLQSRGID--RIDALVSTHADADHIGGhaavIEHF-- 133
Cdd:cd07729    36 LIEHPEG-TILVDTGfhpDAADDPGGlelafppgvteeqtLEEQLARLGLDpeDIDYVILSHLHFDHAGG----LDLFpn 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 134 ------ETEGEgvgAVYDPgVAASTATYDRYLDAVERHDVPLYRTLAGDRIPLDGARVtVLGPPQTPladgerneNSIVL 207
Cdd:cd07729   111 atiivqRAELE---YATGP-DPLAAGYYEDVLALDDDLPGGRVRLVDGDYDLFPGVTL-IPTPGHTP--------GHQSV 177

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1336550306 208 RVEFGRTSVLLPGDAGPVEE-------PYLVDNHEEALD 239
Cdd:cd07729   178 LVRLPEGTVLLAGDAAYTYEnleegrpPGINYDPEAALA 216
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 73-193 1.95e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 42.49  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  73 STLIVGPTgETVLVDTGDFRDDGAYVVDYLQSRGiDRIDALVSTHADADHIGGHAAVIEHFetegEGVGAVYDPGVAAS- 151
Cdd:cd07739    18 STLIYGET-EAVLVDAQFTRADAERLADWIKASG-KTLTTIYITHGHPDHYFGLEVLLEAF----PDAKVVATPAVVAHi 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1336550306 152 TATYD---RYLDAVERHDVP----LYRTLAGDRIPLDGARVTVLGPPQT 193
Cdd:cd07739    92 KAQLEpklAFWGPLLGGNAParlvVPEPLDGDTLTLEGHPLEIVGVGGG 140
NorV COG0426
Flavorubredoxin [Energy production and conversion];
75-133 2.23e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 43.28  E-value: 2.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336550306  75 LIVGptGETVLVDTGD--FRDDgayVVDYLQSR-GIDRIDALVSTHADADHIGGHAAVIEHF 133
Cdd:COG0426    38 LIVD--EKTALIDTVGesFFEE---FLENLSKViDPKKIDYIIVNHQEPDHSGSLPELLELA 94
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 81-227 2.73e-04

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 42.57  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  81 GETVLVDTG-DFRDDGAyvvdyLQSRGIDRIDALVSTHADADHIGGHAAVIEHFETEGegvGAVY-DPGVAASTATYDRY 158
Cdd:COG1235    44 GTRLLIDAGpDLREQLL-----RLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNP---IPVYaTPGTLEALERRFPY 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336550306 159 LDAVERHDVPLYRTLAGDRIPLDGARVT---VLGPPQTPLAdgernensivLRVEFGRTSVLLPGDAGPVEE 227
Cdd:COG1235   116 LFAPYPGKLEFHEIEPGEPFEIGGLTVTpfpVPHDAGDPVG----------YRIEDGGKKLAYATDTGYIPE 177
PRK11539 PRK11539
ComEC family competence protein; Provisional
 63-310 8.70e-04

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 41.90  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  63 VHFINVGQGDSTLIVgPTGETVLVDTGDFRDDGA----YVVDYLQSRGIDrIDALVSTHADADHIGGHAAVIEHFetege 138
Cdd:PRK11539  503 VDMLDVGHGLAVVIE-RNGKAILYDTGNAWPTGDsaqqVIIPWLRWHGLT-PEGIILSHEHLDHRGGLASLLHAW----- 575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 139 gvgavydPGVAASTATYdryldavERHDVPLYRtlaGDRIPLDGARVTVLGPPQTPLADGerNENSIVLRVEFGRTSVLL 218
Cdd:PRK11539  576 -------PMAWIRSPLN-------WANHLPCVR---GEQWQWQGLTFSVHWPLEQSNDAG--NNDSCVIRVDDGKHSILL 636

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 219 PGDAGPVEEPYLVDNHEEALDVTLLKAGHHGSSSSTSAALLNAATPKAVVVSSAYDSRYGHPHEEVLGRLASRSIPTYWT 298
Cdd:PRK11539  637 TGDLEAQAEQKLLSRYWQQLAATLLQVPHHGSNTSSSLPFIRAVNGKVALASASRYNAWRLPSVKVKQRYQQQGYQWRDT 716

                         250
                  ....*....|....
gi 1336550306 299 ATHG--TVVATSDG 310
Cdd:PRK11539  717 PHSGqlSVYFSADG 730
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 75-133 9.73e-04

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 40.55  E-value: 9.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336550306  75 LIVGptGETVLVDTGD--FRDDgayVVDYLQSR-GIDRIDALVSTHADADHIGGHAAVIEHF 133
Cdd:cd07709    36 LIKD--EKTALIDTVKepFFDE---FLENLEEViDPRKIDYIVVNHQEPDHSGSLPELLELA 92
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 81-125 1.83e-03

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 39.84  E-value: 1.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1336550306  81 GETVLVDTG---DFRDDGAYVVDYLQSRGIDR--IDALVSTHADADHIGG 125
Cdd:cd07720    58 GRLILVDTGaggLFGPTAGKLLANLAAAGIDPedIDDVLLTHLHPDHIGG 107
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 83-227 3.05e-03

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 38.83  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  83 TVLVDTG-DFRDDGAYVVDYLQSRGiDRIDALVSTHADADHIGGHAAVIEHFETEgegvgaVY-DPGVAASTATYDRYLD 160
Cdd:pfam12706   2 RILIDPGpDLRQQALPALQPGRLRD-DPIDAVLLTHDHYDHLAGLLDLREGRPRP------LYaPLGVLAHLRRNFPYLF 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 161 AVERHDVPLYRTLAGDRIPLDGARVTVLGPPQ---TPLADGERNENSIVLRVEFGRTSVLLPGDAGPVEE 227
Cdd:pfam12706  75 LLEHYGVRVHEIDWGESFTVGDGGLTVTATPArhgSPRGLDPNPGDTLGFRIEGPGKRVYYAGDTGYFPD 144
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 80-232 3.35e-03

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 39.78  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  80 TGETVLVDTGDFRddgaYVVDYLQSRGIDR------------IDALVSTHADADHIG-GHAAVIEHFEtegegvGAVYdp 146
Cdd:COG1236    13 TGSCYLLETGGTR----ILIDCGLFQGGKErnwppfpfrpsdVDAVVLTHAHLDHSGaLPLLVKEGFR------GPIY-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306 147 gvaASTATYD----RYLDAV-----ERHDVPLY------------RTLA-GDRIPLDGARVT------VLGppqtpladg 198
Cdd:COG1236    81 ---ATPATADlariLLGDSAkiqeeEAEAEPLYteedaeralelfQTVDyGEPFEIGGVRVTfhpaghILG--------- 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1336550306 199 ernenSIVLRVEFGRTSVLLPGDAGPVEEPYLVD 232
Cdd:COG1236   149 -----SAQVELEVGGKRIVFSGDYGREDDPLLAP 177
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 76-132 4.29e-03

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 38.05  E-value: 4.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  76 IVGPTGETVLVDTG-DFRDDGAYVVDYLQSRGID--RIDALVSTHADADHIGGhAAVIEH 132
Cdd:cd07725    19 LLRDGDETTLIDTGlATEEDAEALWEGLKELGLKpsDIDRVLLTHHHPDHIGL-AGKLQE 77
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 73-133 5.95e-03

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 37.95  E-value: 5.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336550306  73 STLIVGPtGETVLVDTGDFRDdGAYVVDYLQSRGI--DRIDALVSTHADADHIGG-----HAAVIEHF 133
Cdd:cd07711    24 VTLIKDG-GKNILVDTGTPWD-RDLLLKALAEHGLspEDIDYVVLTHGHPDHIGNlnlfpNATVIVGW 89
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 73-131 8.48e-03

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 37.87  E-value: 8.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336550306  73 STLIVGPTGeTVLVDTGDFRDDGAYVVDYLQSRGIDR-IDALVSTHADADHIGGHAAVIE 131
Cdd:cd07710    20 MTFIEGDTG-LIIIDTLESAEAAKAALELFRKHTGDKpVKAIIYTHSHPDHFGGAGGFVE 78
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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